Evidence map›Paper›PMID 32193574›Full record

ArticleApplied microbiology and biotechnology2020

Characterisation of four hotdog-fold thioesterases for their implementation in a novel organic acid production system.

T W P Hickman, D Baud, L Benhamou, H C Hailes, J M Ward

Open access · hybridAbstract read
In one paragraph

Article in Applied microbiology and biotechnology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.3field-weighted citation impact, top 44% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

3 citing papers in PubMed, 5 citations in OpenAlex.

  1. Article
  2. Thioesterase enzyme families: Functions, structures, and mechanisms.Protein science : a publication of the Protein Society · 2022
    Article
  3. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 1 institution in 1 country.

T W P HickmanDepartment of Biochemical Engineering, University College London, Gower Street, London, WC1E 6BT, UK.
D BaudDepartment of Chemistry, University College London, 20 Gordon Street, London, WC1H 0AJ, UK.
L BenhamouDepartment of Chemistry, University College London, 20 Gordon Street, London, WC1H 0AJ, UK.
H C HailesDepartment of Chemistry, University College London, 20 Gordon Street, London, WC1H 0AJ, UK.
J M WardDepartment of Biochemical Engineering, University College London, Gower Street, London, WC1E 6BT, UK. j.ward@ucl.ac.uk.
University College London · GB

Funding

Biotechnology and Biological Sciences Research Council BB/L007444/1Biotechnology and Biological Sciences Research Council BB/N01877X/1
6 · The paper itself

Abstract

With increasing interest in the diverse properties of organic acids and their application in synthetic pathways, developing biological tools for producing known and novel organic acids would be very valuable. In such a system, organic acids may be activated as coenzyme A (CoA) esters, then modified by CoA-dependent enzymes, followed by CoA liberation by a broad-acting thioesterase. This study has focused on the identification of suitable thioesterases (TE) for utilisation in such a pathway. Four recombinant hotdog-fold TEs were screened with a range of CoA esters in order to identify a highly active, broad spectrum TE. The TesB-like TE, RpaL, from Rhodopseudomonas palustris was found to be able to use aromatic, alicyclic and both long and short aliphatic CoA esters. Size exclusion chromatography, revealed RpaL to be a monomer of fused hotdog domains, in contrast to the complex quaternary structures found with similar TesB-like TEs. Nonetheless, sequence alignments showed a conserved catalytic triad despite the variation in quaternary arrangement. Kinetic analysis revealed a preference towards short-branched chain CoA esters with the highest specificity towards DL-β-hydroxybutyryl CoA (1.6 × 10

Indexed as

Amino Acid SequenceCoenzyme ACrystallography, X-RayKineticsModels, MolecularPseudomonas aeruginosaRhodopseudomonasSubstrate SpecificityThiolester HydrolasesCoenzyme AThiolester HydrolasesCoAOrganic acidPromiscuousRpaLThioesterase

Identifiers

PMID32193574
PMCPMC7190597
OpenAlexW3011597703

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.